ID DCOR_HUMAN Reviewed; 461 AA. AC P11926; Q53TU3; Q6LDS9; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 27-MAR-2024, entry version 232. DE RecName: Full=Ornithine decarboxylase; DE Short=ODC; DE EC=4.1.1.17 {ECO:0000269|PubMed:17407445}; GN Name=ODC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3595418; DOI=10.1089/dna.1987.6.179; RA Hickok N.J., Seppaenen P.J., Gunsalus G.L., Jaenne O.A.; RT "Complete amino acid sequence of human ornithine decarboxylase deduced from RT complementary DNA."; RL DNA 6:179-187(1987). RN [2] RP SEQUENCE REVISION TO 415. RA Jaenne O.A.; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2693021; DOI=10.1089/dna.1.1989.8.623; RA Fitzgerald M.C., Flanagan M.A.; RT "Characterization and sequence analysis of the human ornithine RT decarboxylase gene."; RL DNA 8:623-634(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2587220; DOI=10.1093/nar/17.21.8855; RA van Steeg H., van Oostrom C.T.M., Martens J.W.M., van Kreyl C.F., RA Schepens J., Wieringa B.; RT "Nucleotide sequence of the human ornithine decarboxylase gene."; RL Nucleic Acids Res. 17:8855-8856(1989). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2227439; DOI=10.1016/0378-1119(90)90233-h; RA Hickok N.J., Wahlfors J., Crozat A., Halmekytoe M., Alhonen L., Jaenne J., RA Jaenne O.A.; RT "Human ornithine decarboxylase-encoding loci: nucleotide sequence of the RT expressed gene and characterization of a pseudogene."; RL Gene 93:257-263(1990). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2318872; DOI=10.1016/s0021-9258(19)34057-8; RA Moshier J.A., Gilbert J.D., Skunca M., Dosescu J., Almodovar K.M., RA Luk G.D.; RT "Isolation and expression of a human ornithine decarboxylase gene."; RL J. Biol. Chem. 265:4884-4892(1990). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1598217; DOI=10.1093/nar/20.10.2581; RA Moshier J.A., Osborne D.L., Skunca M., Dosescu J., Gilbert J.D., RA Fitzgerald M.C., Polidori G., Wagner R.L., Friezner Degen S.J., Luk G.D., RA Flanagan M.A.; RT "Multiple promoter elements govern expression of the human ornithine RT decarboxylase gene in colon carcinoma cells."; RL Nucleic Acids Res. 20:2581-2590(1992). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8519686; RA Wright P.S., Cooper J.R., Cross-Doersen D.E., Miller J.A., RA Chmielewski P.A., Wagner R.L., Streng K.A., Flanagan M.A.; RT "Regulation of ornithine decarboxylase mRNA levels in human breast cancer RT cells: pattern of expression and involvement of core enhancer promoter RT element."; RL Cell Growth Differ. 6:1097-1102(1995). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Esophagus, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-22. RX PubMed=2317811; RA Hsieh J.T., Denning M.F., Heidel S.M., Verma A.K.; RT "Expression of human chromosome 2 ornithine decarboxylase gene in ornithine RT decarboxylase-deficient Chinese hamster ovary cells."; RL Cancer Res. 50:2239-2244(1990). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-461. RX PubMed=3308908; DOI=10.1002/jcp.1041320318; RA Kaczmarek L., Calabretta B., Ferrari S., de Riel J.K.; RT "Cell-cycle-dependent expression of human ornithine decarboxylase."; RL J. Cell. Physiol. 132:545-551(1987). RN [16] RP S-NITROSYLATION. RX PubMed=10462479; DOI=10.1006/bbrc.1999.1210; RA Bauer P.M., Fukuto J.M., Buga G.M., Pegg A.E., Ignarro L.J.; RT "Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation."; RL Biochem. Biophys. Res. Commun. 262:355-358(1999). RN [17] RP S-NITROSYLATION AT CYS-360, AND MUTAGENESIS OF CYS-360. RX PubMed=11461922; DOI=10.1074/jbc.m105219200; RA Bauer P.M., Buga G.M., Fukuto J.M., Pegg A.E., Ignarro L.J.; RT "Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of RT cysteine 360 in the active site of the enzyme."; RL J. Biol. Chem. 276:34458-34464(2001). RN [18] RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x; RA Leong W.F., Chow V.T.; RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal RT differential cellular gene expression in response to enterovirus 71 RT infection."; RL Cell. Microbiol. 8:565-580(2006). RN [19] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=17900240; DOI=10.1042/bj20071004; RA Kanerva K., Makitie L.T., Pelander A., Heiskala M., Andersson L.C.; RT "Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor RT but not an arginine decarboxylase."; RL Biochem. J. 409:187-192(2008). RN [20] {ECO:0007744|PDB:1D7K} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 7-427, AND SUBUNIT. RX PubMed=10623504; DOI=10.1006/jmbi.1999.3331; RA Almrud J.J., Oliveira M.A., Kern A.D., Grishin N.V., Phillips M.A., RA Hackert M.L.; RT "Crystal structure of human ornithine decarboxylase at 2.1 A resolution: RT structural insights to antizyme binding."; RL J. Mol. Biol. 295:7-16(2000). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH COFACTOR AND RP SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17407445; DOI=10.1042/bj20070188; RA Dufe V.T., Ingner D., Heby O., Khomutov A.R., Persson L., Al-Karadaghi S.; RT "A structural insight into the inhibition of human and Leishmania donovani RT ornithine decarboxylases by 1-amino-oxy-3-aminopropane."; RL Biochem. J. 405:261-268(2007). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 2-421 IN COMPLEX WITH COFACTOR RP AND OAZ1. RX PubMed=26305948; DOI=10.1073/pnas.1508187112; RA Wu H.Y., Chen S.F., Hsieh J.Y., Chou F., Wang Y.H., Lin W.T., Lee P.Y., RA Yu Y.J., Lin L.Y., Lin T.S., Lin C.L., Liu G.Y., Tzeng S.R., Hung H.C., RA Chan N.L.; RT "Structural basis of antizyme-mediated regulation of polyamine RT homeostasis."; RL Proc. Natl. Acad. Sci. U.S.A. 112:11229-11234(2015). RN [23] RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH COFACTOR; OAZ1 AND RP INHIBITOR. RX PubMed=26443277; DOI=10.1038/srep14738; RA Wu D., Kaan H.Y., Zheng X., Tang X., He Y., Vanessa Tan Q., Zhang N., RA Song H.; RT "Structural basis of ornithine decarboxylase inactivation and accelerated RT degradation by polyamine sensor antizyme1."; RL Sci. Rep. 5:14738-14738(2015). RN [24] RP VARIANT BABS 448-LYS--VAL-461 DEL, INVOLVEMENT IN BABS, AND RP CHARACTERIZATION OF VARIANT BABS 448-LYS--VAL-461 DEL. RX PubMed=30239107; DOI=10.1002/ajmg.a.40523; RA Bupp C.P., Schultz C.R., Uhl K.L., Rajasekaran S., Bachmann A.S.; RT "Novel de novo pathogenic variant in the ODC1 gene in a girl with RT developmental delay, alopecia, and dysmorphic features."; RL Am. J. Med. Genet. A 176:2548-2553(2018). RN [25] RP VARIANT BABS 419-GLN--VAL-461 DEL, AND INVOLVEMENT IN BABS. RX PubMed=30475435; DOI=10.1002/ajmg.a.60677; RA Rodan L.H., Anyane-Yeboa K., Chong K., Klein Wassink-Ruiter J.S., RA Wilson A., Smith L., Kothare S.V., Rajabi F., Blaser S., Ni M., RA DeBerardinis R.J., Poduri A., Berry G.T.; RT "Gain-of-function variants in the ODC1 gene cause a syndromic RT neurodevelopmental disorder associated with macrocephaly, alopecia, RT dysmorphic features, and neuroimaging abnormalities."; RL Am. J. Med. Genet. A 176:2554-2560(2018). CC -!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine CC biosynthesis that converts ornithine into putrescine, which is the CC precursor for the polyamines, spermidine and spermine. Polyamines are CC essential for cell proliferation and are implicated in cellular CC processes, ranging from DNA replication to apoptosis. CC {ECO:0000269|PubMed:17900240}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, CC ChEBI:CHEBI:326268; EC=4.1.1.17; CC Evidence={ECO:0000269|PubMed:17407445}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:26443277}; CC -!- ACTIVITY REGULATION: Inhibited by S-nitrosylation (PubMed:10462479, CC PubMed:11461922). Inhibited by antizymes (AZs) OAZ1, OAZ2 and OAZ3 in CC response to polyamine levels. AZs inhibit the assembly of the CC functional homodimer by binding to ODC monomers. Additionally, OAZ1 CC targets ODC monomers for ubiquitin-independent proteolytic destruction CC by the 26S proteasome (PubMed:17900240). Inhibited by 1-amino-oxy-3- CC aminopropane (APA, an isosteric analog of putrescine) CC (PubMed:17407445). Irreversibly inhibited by alpha- CC difluoromethylornithine (DFMO) (PubMed:17407445). CC {ECO:0000269|PubMed:10462479, ECO:0000269|PubMed:11461922, CC ECO:0000269|PubMed:17407445, ECO:0000269|PubMed:17900240}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.08 mM for L-ornithine {ECO:0000269|PubMed:17407445}; CC Note=kcat is 3.3 sec(-1) with L-ornithine as substrate. CC {ECO:0000269|PubMed:17407445}; CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via CC L-ornithine pathway; putrescine from L-ornithine: step 1/1. CC -!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the CC active sites are constructed of residues from both monomers (Probable). CC Does not form a heterodimer with AZIN2 (By similarity). CC {ECO:0000250|UniProtKB:P00860, ECO:0000305|PubMed:10623504}. CC -!- INTERACTION: CC P11926; Q9H8Y8: GORASP2; NbExp=11; IntAct=EBI-1044287, EBI-739467; CC P11926; Q92993: KAT5; NbExp=6; IntAct=EBI-1044287, EBI-399080; CC P11926; Q9UMX2: OAZ3; NbExp=5; IntAct=EBI-1044287, EBI-10281601; CC P11926; Q9UMX2-2: OAZ3; NbExp=3; IntAct=EBI-1044287, EBI-12049527; CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71) CC infection (at protein level). {ECO:0000269|PubMed:16548883}. CC -!- PTM: S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 CC cysteine residues. {ECO:0000269|PubMed:10462479, CC ECO:0000269|PubMed:11461922}. CC -!- DISEASE: Bachmann-Bupp syndrome (BABS) [MIM:619075]: An autosomal CC dominant disorder characterized by global developmental delay, CC alopecia, absolute or relative macrocephaly, and facial dysmorphism. CC Neuroimaging shows white matter abnormalities, prominent Virchow-Robin CC spaces, periventricular cysts, and abnormalities of the corpus CC callosum. {ECO:0000269|PubMed:30239107, ECO:0000269|PubMed:30475435}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. BABS is due to truncating variants that lead to a gain CC of function. This phenomenon apparently results from truncation CC proximal to or involving the C-terminal region of ODC1 protein, distal CC enough to allow escape from nonsense-mediated decay. A gain of function CC is corroborated by elevated plasma levels of N-acetylputrescine, with CC otherwise normal polyamine levels, in affected individuals. CC {ECO:0000269|PubMed:30475435}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/odc1/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ornithine decarboxylase entry; CC URL="https://en.wikipedia.org/wiki/Ornithine_decarboxylase"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M16650; AAA59966.2; -; mRNA. DR EMBL; M31061; AAA60563.1; -; Genomic_DNA. DR EMBL; X16277; CAA34353.1; -; Genomic_DNA. DR EMBL; M33764; AAA60564.1; -; Genomic_DNA. DR EMBL; M34158; AAA59969.1; -; Genomic_DNA. DR EMBL; M81740; AAA59967.1; -; Genomic_DNA. DR EMBL; X55362; CAA39047.1; -; mRNA. DR EMBL; AK292352; BAF85041.1; -; mRNA. DR EMBL; AK312766; BAG35632.1; -; mRNA. DR EMBL; AY841870; AAV88093.1; -; Genomic_DNA. DR EMBL; AC007249; AAY15034.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00958.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00959.1; -; Genomic_DNA. DR EMBL; BC025296; AAH25296.1; -; mRNA. DR EMBL; X53271; CAA37369.1; -; mRNA. DR EMBL; M20372; AAA59968.1; -; mRNA. DR CCDS; CCDS1672.1; -. DR PIR; S06900; DCHUO. DR RefSeq; NP_001274118.1; NM_001287189.1. DR RefSeq; NP_001274119.1; NM_001287190.1. DR RefSeq; NP_002530.1; NM_002539.2. DR PDB; 1D7K; X-ray; 2.10 A; A/B=7-427. DR PDB; 2ON3; X-ray; 3.00 A; A/B=1-461. DR PDB; 2OO0; X-ray; 1.90 A; A/B=1-461. DR PDB; 4ZGY; X-ray; 2.63 A; A=2-421. DR PDB; 5BWA; X-ray; 3.20 A; A=1-461. DR PDB; 7S3F; X-ray; 2.49 A; A/B=1-424. DR PDB; 7S3G; X-ray; 1.66 A; A/B=1-424. DR PDB; 7U6P; X-ray; 2.35 A; A/B=1-424. DR PDB; 7U6U; X-ray; 1.85 A; A/B=1-424. DR PDBsum; 1D7K; -. DR PDBsum; 2ON3; -. DR PDBsum; 2OO0; -. DR PDBsum; 4ZGY; -. DR PDBsum; 5BWA; -. DR PDBsum; 7S3F; -. DR PDBsum; 7S3G; -. DR PDBsum; 7U6P; -. DR PDBsum; 7U6U; -. DR AlphaFoldDB; P11926; -. DR SMR; P11926; -. DR BioGRID; 111007; 23. DR CORUM; P11926; -. DR IntAct; P11926; 17. DR MINT; P11926; -. DR STRING; 9606.ENSP00000234111; -. DR BindingDB; P11926; -. DR ChEMBL; CHEMBL1869; -. DR DrugBank; DB06243; Eflornithine. DR DrugBank; DB04263; Geneticin. DR DrugBank; DB03856; L-Eflornithine. DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine. DR DrugBank; DB02824; N-Pyridoxyl-Glycine-5-Monophosphate. DR DrugBank; DB01917; Putrescine. DR DrugBank; DB00114; Pyridoxal phosphate. DR DrugBank; DB02209; Pyridoxine phosphate. DR DrugBank; DB00203; Sildenafil. DR DrugBank; DB00127; Spermine. DR DrugBank; DB00313; Valproic acid. DR DrugCentral; P11926; -. DR GuidetoPHARMACOLOGY; 1276; -. DR iPTMnet; P11926; -. DR PhosphoSitePlus; P11926; -. DR BioMuta; ODC1; -. DR DMDM; 118377; -. DR EPD; P11926; -. DR jPOST; P11926; -. DR MassIVE; P11926; -. DR PaxDb; 9606-ENSP00000234111; -. DR PeptideAtlas; P11926; -. DR ProteomicsDB; 52813; -. DR Pumba; P11926; -. DR Antibodypedia; 781; 974 antibodies from 34 providers. DR CPTC; P11926; 3 antibodies. DR DNASU; 4953; -. DR Ensembl; ENST00000234111.9; ENSP00000234111.4; ENSG00000115758.14. DR Ensembl; ENST00000405333.5; ENSP00000385333.1; ENSG00000115758.14. DR Ensembl; ENST00000443218.2; ENSP00000390691.2; ENSG00000115758.14. DR Ensembl; ENST00000699835.1; ENSP00000514633.1; ENSG00000115758.14. DR Ensembl; ENST00000699836.1; ENSP00000514634.1; ENSG00000115758.14. DR GeneID; 4953; -. DR KEGG; hsa:4953; -. DR MANE-Select; ENST00000234111.9; ENSP00000234111.4; NM_002539.3; NP_002530.1. DR UCSC; uc002rao.3; human. DR AGR; HGNC:8109; -. DR CTD; 4953; -. DR DisGeNET; 4953; -. DR GeneCards; ODC1; -. DR GeneReviews; ODC1; -. DR HGNC; HGNC:8109; ODC1. DR HPA; ENSG00000115758; Low tissue specificity. DR MalaCards; ODC1; -. DR MIM; 165640; gene. DR MIM; 619075; phenotype. DR neXtProt; NX_P11926; -. DR OpenTargets; ENSG00000115758; -. DR Orphanet; 544488; Global developmental delay-alopecia-macrocephaly-facial dysmorphism-structural brain anomalies syndrome. DR PharmGKB; PA31897; -. DR VEuPathDB; HostDB:ENSG00000115758; -. DR eggNOG; KOG0622; Eukaryota. DR GeneTree; ENSGT00950000182995; -. DR HOGENOM; CLU_026444_1_1_1; -. DR InParanoid; P11926; -. DR OMA; AYCRSMA; -. DR OrthoDB; 48358at2759; -. DR PhylomeDB; P11926; -. DR TreeFam; TF300760; -. DR BioCyc; MetaCyc:HS03935-MONOMER; -. DR BRENDA; 4.1.1.17; 2681. DR PathwayCommons; P11926; -. DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-HSA-351202; Metabolism of polyamines. DR SABIO-RK; P11926; -. DR SignaLink; P11926; -. DR SIGNOR; P11926; -. DR UniPathway; UPA00535; UER00288. DR BioGRID-ORCS; 4953; 22 hits in 1174 CRISPR screens. DR ChiTaRS; ODC1; human. DR EvolutionaryTrace; P11926; -. DR GeneWiki; ODC1; -. DR GenomeRNAi; 4953; -. DR Pharos; P11926; Tclin. DR PRO; PR:P11926; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P11926; Protein. DR Bgee; ENSG00000115758; Expressed in secondary oocyte and 207 other cell types or tissues. DR ExpressionAtlas; P11926; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004586; F:ornithine decarboxylase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; ISS:UniProtKB. DR GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR CDD; cd00622; PLPDE_III_ODC; 1. DR DisProt; DP02673; -. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR022643; De-COase2_C. DR InterPro; IPR022657; De-COase2_CS. DR InterPro; IPR022644; De-COase2_N. DR InterPro; IPR022653; De-COase2_pyr-phos_BS. DR InterPro; IPR000183; Orn/DAP/Arg_de-COase. DR InterPro; IPR002433; Orn_de-COase. DR InterPro; IPR029066; PLP-binding_barrel. DR PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1. DR PANTHER; PTHR11482:SF42; ORNITHINE DECARBOXYLASE; 1. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01179; ODADCRBXLASE. DR PRINTS; PR01182; ORNDCRBXLASE. DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1. DR SUPFAM; SSF51419; PLP-binding barrel; 1. DR PROSITE; PS00878; ODR_DC_2_1; 1. DR PROSITE; PS00879; ODR_DC_2_2; 1. DR Genevisible; P11926; HS. PE 1: Evidence at protein level; KW 3D-structure; Decarboxylase; Disease variant; Hypotrichosis; Lyase; KW Phosphoprotein; Polyamine biosynthesis; Pyridoxal phosphate; KW Reference proteome; S-nitrosylation. FT CHAIN 1..461 FT /note="Ornithine decarboxylase" FT /id="PRO_0000149891" FT ACT_SITE 360 FT /note="Proton donor; shared with dimeric partner" FT /evidence="ECO:0000305|PubMed:10623504" FT BINDING 200 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:17407445, FT ECO:0007744|PDB:2OO0" FT BINDING 237 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:17407445, FT ECO:0007744|PDB:2OO0" FT BINDING 274..277 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:17407445, FT ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277, FT ECO:0007744|PDB:2OO0" FT BINDING 331..332 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 361 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P07805" FT BINDING 389 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:17407445, FT ECO:0000269|PubMed:26305948, ECO:0000269|PubMed:26443277, FT ECO:0007744|PDB:2OO0" FT SITE 197 FT /note="Stacks against the aromatic ring of pyridoxal FT phosphate and stabilizes reaction intermediates" FT /evidence="ECO:0000250|UniProtKB:P00860" FT MOD_RES 69 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000269|PubMed:26305948, FT ECO:0000305|PubMed:17407445" FT MOD_RES 303 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250|UniProtKB:P00860" FT MOD_RES 360 FT /note="S-nitrosocysteine; in inhibited form" FT /evidence="ECO:0000305|PubMed:11461922" FT VARIANT 419..461 FT /note="Missing (in BABS)" FT /evidence="ECO:0000269|PubMed:30475435" FT /id="VAR_085000" FT VARIANT 448..461 FT /note="Missing (in BABS; gain-of-function variant resulting FT in increased putrescine biosynthesis as indicated by higher FT amount of putrescine in patient red blood cells compared to FT controls; increased ODC1 protein levels in patient red FT blood cells)" FT /evidence="ECO:0000269|PubMed:30239107" FT /id="VAR_085001" FT MUTAGEN 360 FT /note="C->A: 25% decrease of in vitro nitrosylation level." FT /evidence="ECO:0000269|PubMed:11461922" FT HELIX 1..5 FT /evidence="ECO:0007829|PDB:2OO0" FT TURN 7..9 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 20..30 FT /evidence="ECO:0007829|PDB:7S3G" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 45..58 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 74..83 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 92..100 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 117..125 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 136..145 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:2OO0" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:7U6U" FT HELIX 174..186 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 206..225 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 240..246 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 248..262 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 270..273 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 277..280 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 284..297 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 312..319 FT /evidence="ECO:0007829|PDB:7S3G" FT TURN 322..324 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 328..331 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:7U6U" FT STRAND 350..356 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 365..373 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 380..383 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:7S3G" FT STRAND 404..410 FT /evidence="ECO:0007829|PDB:7S3G" FT HELIX 411..421 FT /evidence="ECO:0007829|PDB:7S3G" SQ SEQUENCE 461 AA; 51148 MW; 8CCB88CE80E823C5 CRC64; MNNFGNEEFD CHFLDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK KHLRWLKALP RVTPFYAVKC NDSKAIVKTL AATGTGFDCA SKTEIQLVQS LGVPPERIIY ANPCKQVSQI KYAANNGVQM MTFDSEVELM KVARAHPKAK LVLRIATDDS KAVCRLSVKF GATLRTSRLL LERAKELNID VVGVSFHVGS GCTDPETFVQ AISDARCVFD MGAEVGFSMY LLDIGGGFPG SEDVKLKFEE ITGVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKIVLKEQ TGSDDEDESS EQTFMYYVND GVYGSFNCIL YDHAHVKPLL QKRPKPDEKY YSSSIWGPTC DGLDRIVERC DLPEMHVGDW MLFENMGAYT VAAASTFNGF QRPTIYYVMS GPAWQLMQQF QNPDFPPEVE EQDASTLPVS CAWESGMKRH RAACASASIN V //